Dynamic energy correlation analysis of E. coli aspartokinase III and alteration of allosteric regulation by manipulating energy transduction pathways

Publikationstyp
Journal Article
Date Issued
2021-03-02
Sprache
English
Author(s)
Wang, Shizhen  
Ma, Cheng-Wei  
Zeng, An-Ping  orcid-logo
Institut
Bioprozess- und Biosystemtechnik V-1  
TORE-DOI
10.15480/882.3538
TORE-URI
http://hdl.handle.net/11420/9550
Journal
Engineering in life sciences  
Volume
21
Issue
5
Start Page
314
End Page
323
Citation
Engineering in Life Sciences 21 (5): 314-323 (2021-05-01)
Publisher DOI
10.1002/elsc.202000065
Scopus ID
2-s2.0-85101881785
Publisher
Wiley-Blackwell
Conformational change associated with allosteric regulation in a protein is ultimately driven by energy transformation. However, little is known about the latter process. In this work, we combined steered molecular dynamics simulations and sequence conservation analysis to investigate the conformational changes and energy transformation in the allosteric enzyme aspartokinase III (AK III) from Escherichia coli. Correlation analysis of energy change at residue level indicated significant transformation between electrostatic energy and dihedral angle energy during the allosteric regulation. Key amino acid residues located in the corresponding energy transduction pathways were identified by dynamic energy correlation analysis. To verify their functions, residues with a high energy correlation in the pathways were altered and their effects on allosteric regulation of AKIII were determined. This study sheds new insights into energy transformation during allosteric regulation of AK III and proposes a strategy to identify key residues that are involved in intramolecular energy transduction and thus in driving the allosteric process.
Subjects
allosteric regulation
aspartokinase III
dynamic energy correlation
energy redistribution
energy transduction pathway
DDC Class
570: Biowissenschaften, Biologie
600: Technik
Funding(s)
Publikationsfonds 2021  
Funding Organisations
Deutscher Akademischer Austauschdienst  
National Natural Science Foundation of China  
More Funding Information
The authors gratefully acknowledge the support of K. C. Wong Education Foundation and DAAD (no. 91700128). This work was also supported by the National Natural Science Foundation of China (no. 21776233, 22078273), Natural Science Foundation of Fujian Province of China (No. 2018J01013), Fundamental Research Funds for the Central Universities (no. 20720200038, 20720170033).
Publication version
publishedVersion
Lizenz
https://creativecommons.org/licenses/by/4.0/
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